Cosmic Peptides research library

Mitochondrial-derived peptides

2 peptides compared: their calculated properties, how each relates in sequence to Humanin, and the analytical variants they share.

Last reviewed · Editorial policy

Mitochondrial-derived peptides are encoded by short open reading frames in the mitochondrial genome: MOTS-c in the 12S rRNA region and humanin in the 16S rRNA region. The two are unrelated in sequence.

Members compared

Calculated from each structure
PeptideResiduesFormulaMonoisotopic mass (Da)Charge, pH 7pITermini
MOTS-c16C101H152N28O22S22,173.10773.010.64free amine; free acid
Humanin24C119H204N34O32S22,685.48221.99.82free amine; free acid

Sequences and relationships

Each member's sequence in three-letter code, and how it relates to Humanin, worked out position by position from the structures. Members with no entry in the last column are not direct sequence relatives of Humanin.

Relationship to Humanin
PeptideSequenceRelationship
MOTS-cH-Met-Arg-Trp-Gln-Glu-Met-Gly-Tyr-Ile-Phe-Tyr-Pro-Arg-Lys-Leu-Arg-OH—
HumaninH-Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala-OHReference sequence

Shared analytical features

The sequence-specific variants from each member's entry, counted across the family: what an HPLC or mass spectrometry result for these peptides is most often read against.

Variants by number of members
VariantMembers
Methionine oxidation2 of 2: MOTS-c, Humanin
Free cysteine1 of 2: Humanin
Glutamine deamidation1 of 2: MOTS-c
Tryptophan oxidation1 of 2: MOTS-c

Every member can also carry the synthesis-related variants common to all synthetic peptides, described in How synthetic peptides are made.

Sources & Further Reading

  1. Prohaska T, Irrgeher J, Benefield J, Böhlke JK, Chesson LA, Coplen TB, et al. Standard atomic weights of the elements 2021 (IUPAC Technical Report). Pure and Applied Chemistry 2022;94(5):573–600. doi:10.1515/pac-2019-0603
  2. Wang M, Huang WJ, Kondev FG, Audi G, Naimi S. The AME 2020 atomic mass evaluation (II). Tables, graphs and references. Chinese Physics C 2021;45(3):030003. doi:10.1088/1674-1137/abddaf
  3. Rice P, Longden I, Bleasby A. EMBOSS: the European Molecular Biology Open Software Suite. Trends in Genetics 2000;16(6):276–277. doi:10.1016/S0168-9525(00)02024-2
  4. Pace CN, Vajdos F, Fee L, Grimsley G, Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Science 1995;4(11):2411–2423. doi:10.1002/pro.5560041120
  5. Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology 1982;157(1):105–132. doi:10.1016/0022-2836(82)90515-0
  6. Meija J, Coplen TB, Berglund M, Brand WA, De Bièvre P, Gröning M, et al. Isotopic compositions of the elements 2013 (IUPAC Technical Report). Pure and Applied Chemistry 2016;88(3):293–306. doi:10.1515/pac-2015-0503
  7. Roepstorff P, Fohlman J. Letter to the editors: proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomedical Mass Spectrometry 1984;11(11):601. doi:10.1002/bms.1200111109
  8. Biemann K. Contributions of mass spectrometry to peptide and protein structure. Biomedical and Environmental Mass Spectrometry 1988;16(1–12):99–111. doi:10.1002/bms.1200160119
  9. Geiger T, Clarke S. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. Journal of Biological Chemistry 1987;262(2):785–794. doi:10.1016/S0021-9258(19)75855-4
  10. Manning MC, Chou DK, Murphy BM, Payne RW, Katayama DS. Stability of protein pharmaceuticals: an update. Pharmaceutical Research 2010;27(4):544–575. doi:10.1007/s11095-009-0045-6
  11. D'Hondt M, Bracke N, Taevernier L, Gevaert B, Verbeke F, Wynendaele E, et al. Related impurities in peptide medicines. Journal of Pharmaceutical and Biomedical Analysis 2014;101:2–30. doi:10.1016/j.jpba.2014.06.012

See also

Cite this page

Text

Cosmic Peptides. (2026, October 25). Mitochondrial-derived peptides. Cosmic Peptides Research Library. Retrieved October 26, 2026, from https://cosmicpeptides.com/research/peptides/families/mitochondrial

BibTeX

@misc{cosmicpeptides_research_peptides_families_mitochondrial,
  author       = {{Cosmic Peptides}},
  title        = {Mitochondrial-derived peptides},
  howpublished = {Cosmic Peptides Research Library},
  year         = {2026},
  month        = oct,
  url          = {https://cosmicpeptides.com/research/peptides/families/mitochondrial},
  urldate      = {2026-10-26},
  note         = {Last reviewed 2026-10-25}
}

RIS

TY  - ELEC
AU  - Cosmic Peptides
TI  - Mitochondrial-derived peptides
T2  - Cosmic Peptides Research Library
PB  - Cosmic Peptides
PY  - 2026
DA  - 2026/10/25
UR  - https://cosmicpeptides.com/research/peptides/families/mitochondrial
Y2  - 2026/10/26
LA  - en
ER  -

Cite the date the page was last reviewed, October 25, 2026, as its version. Reference managers such as Zotero can save this page directly.

Changes to this page

  1. Published Peptide reference: 20 more peptides, five new families, five more comparisons

    Opioid peptides, oxytocin and vasopressin, amyloid-β, kinin and angiotensin fragments, hypothalamic and mitochondrial-derived peptides and others, each checked against PubChem; families and comparisons for the new groups.

  2. Published Peptide reference: 15 more peptides and six family pages

    Reference and calibration peptides and relatives of catalog families, each checked against PubChem, and family pages comparing members and showing how each relates in sequence to its family reference.

Changes of substance are listed here; wording changes are not. Every correction is also on the corrections log.

For in vitro laboratory research only. Not for human or veterinary use. This library describes chemistry, analytical methods and published laboratory research; it gives no guidance on use in people or animals.